GenomeNet

Database: UniProt/TrEMBL
Entry: D9TA03_MICAI
LinkDB: D9TA03_MICAI
Original site: D9TA03_MICAI 
ID   D9TA03_MICAI            Unreviewed;       319 AA.
AC   D9TA03;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   01-MAY-2013, entry version 20.
DE   SubName: Full=Deoxyribose-phosphate aldolase;
DE            EC=4.1.2.4;
GN   OrderedLocusNames=Micau_0805;
OS   Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / JCM 10878 /
OS   NBRC 16125 / INA 9442).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micromonosporineae; Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=644283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Hirsch A.M., Woyke T.;
RT   "Complete sequence of Micromonospora aurantiaca ATCC 27029.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes a reversible aldol reaction between
CC       acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-
CC       D-ribose 5-phosphate (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2-deoxy-D-ribose 5-phosphate = D-
CC       glyceraldehyde 3-phosphate + acetaldehyde.
CC   -!- PATHWAY: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate
CC       degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-
CC       deoxy-alpha-D-ribose 1-phosphate: step 2/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002162; ADL44369.1; -; Genomic_DNA.
DR   RefSeq; YP_003833945.1; NC_014391.1.
DR   ProteinModelPortal; D9TA03; -.
DR   EnsemblBacteria; ADL44369; ADL44369; Micau_0805.
DR   GeneID; 9598872; -.
DR   KEGG; mau:Micau_0805; -.
DR   PATRIC; 42387292; VBIMicAur74833_0817.
DR   HOGENOM; HOG000241644; -.
DR   KO; K01619; -.
DR   OMA; MVIDRGA; -.
DR   BioCyc; MAUR644283:GHOD-817-MONOMER; -.
DR   UniPathway; UPA00002; UER00468.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:EC.
DR   GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro.
DR   GO; GO:0046386; P:deoxyribose phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011343; DeoC.
DR   InterPro; IPR002915; DeoC/FbaB/lacD_aldolase.
DR   PANTHER; PTHR10889; PTHR10889; 1.
DR   Pfam; PF01791; DeoC; 1.
DR   PIRSF; PIRSF001357; DeoC; 1.
DR   TIGRFAMs; TIGR00126; deoC; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Lyase; Schiff base.
SQ   SEQUENCE   319 AA;  33768 MW;  A79570A3D620149F CRC64;
     MTATTTSARS DLTELGRSET ALRTFLHGLP GVDQVGAEQR AAQLGTRSIK TTAKAEAIDL
     AIRMVDLTTL EGADTPGKVR ALAAKALRPD PADPSCPHVG AVCVYPSMVP YVAEVLRGSG
     VHLASVATAF PSGQAPLEIK LADVRAAVEA GADEIDMVIN RGAFLAGRYS DVYDEIVATK
     EACGDAHLKV ILETGELATY DNVRRASWLA MLAGGDFIKT STGKVPVAAT LPVTLVMLEA
     VRDFRAATGR QVGVKPAGGI KTTKDAIKYL VMVNETVGAD WLSPDWFRFG ASSLLNDLLM
     QRTKLTTGVY AGPDYFTLD
//
DBGET integrated database retrieval system